EC 2.3.1.157 - Glucosamine-1-phosphate N-acetyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.157

Names

Accepted name:
glucosamine-1-phosphate N-acetyltransferase
Other name:
acetyl-CoA:D-glucosamine-1-phosphate N-acetyltransferase
Systematic name:
acetyl-CoA:α-D-glucosamine-1-phosphate N-acetyltransferase

Reaction

Comments:

The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0019134
UniProtKB/Swiss-Prot: (602) [show] [UniProt]

References

  1. Mengin-Lecreulx, D. and van Heijenoort, J.
    Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis.
    J. Bacteriol. 176: 5788-5795 (1994). [PMID: 8083170]
  2. Gehring, A. M., Lees, W. J., Mindiola, D. J., Walsh, C. T., Brown, E. D.
    Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
    Biochemistry 35: 579-585 (1996). [PMID: 8555230]
  3. Olsen, L. R., Roderick, S. L.
    Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
    Biochemistry 40: 1913-1921 (2001). [PMID: 11329257]

[EC 2.3.1.157 created 2001]